Amino acid sequences around the pyridoxal-5'-phosphate-binding sites of phenol hydroxylase.
Phenol hydroxylase was labelled with pyridoxal 5'-phosphate. A radioactive label was introduced by using sodium boro[3H]hydride to reduce the initially formed Schiff's base. The labelled enzyme was digested with Staphylococcus V8 protease. Labelled peptides were isolated and their sequences were determined. The label could be located to three different lysyl residues. Sequence similarities with the known structures of p-hydroxybenzoate hydroxylase and glutathione reductase are discussed. The positions of the labelled sequences, relative to the bound ligands at the active site, are proposed on the basis of such sequence similarities.
Sejlitz
T
T
Department of Biochemistry and Biotechnology, Royal Institute of Technology, Stockholm, Sweden.
Wernstedt
C
C
Engström
A
A
Neujahr
H Y
HY
D000595:Amino Acid Sequence; D001665:Binding Sites; D003545:Cysteine; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases; D014250:Trichosporon / Q000201:enzymology
D010446:Peptide Fragments; D011732:Pyridoxal Phosphate; D006899:Mixed Function Oxygenases; C022336:phenol 2-monooxygenase; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D003545:Cysteine